H2A2C_BOVIN - dbPTM
H2A2C_BOVIN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2A2C_BOVIN
UniProt AC A1A4R1
Protein Name Histone H2A type 2-C
Gene Name HIST2H2AC
Organism Bos taurus (Bovine).
Sequence Length 129
Subcellular Localization Nucleus. Chromosome.
Protein Description Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling..
Protein Sequence MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHKAKSK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSGRGKQGG
------CCCCCCCCH
36.881500420
2Acetylation------MSGRGKQGG
------CCCCCCCCH
36.88-
4Citrullination----MSGRGKQGGKA
----CCCCCCCCHHH
41.66-
4Methylation----MSGRGKQGGKA
----CCCCCCCCHHH
41.66-
4Citrullination----MSGRGKQGGKA
----CCCCCCCCHHH
41.66-
6Acetylation--MSGRGKQGGKARA
--CCCCCCCCHHHHH
44.39-
6Other--MSGRGKQGGKARA
--CCCCCCCCHHHHH
44.39-
10SuccinylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.34-
10OtherGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.34-
10LactoylationGRGKQGGKARAKAKS
CCCCCCHHHHHHHHH
41.34-
37CrotonylationRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
37OtherRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
37N6-crotonyl-L-lysineRVHRLLRKGNYAERV
HHHHHHHCCCHHHHC
52.02-
75OtherGNAARDNKKTRIIPR
CHHHHCCCCCCEEHH
60.87-
76OtherNAARDNKKTRIIPRH
HHHHCCCCCCEEHHH
49.65-
96OtherRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE
58.68-
96GlutarylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE
58.68-
96SuccinylationRNDEELNKLLGKVTI
CCHHHHHHHHCCEEE
58.68-
100GlutarylationELNKLLGKVTIAQGG
HHHHHHCCEEECCCC
35.85-
105MethylationLGKVTIAQGGVLPNI
HCCEEECCCCCCCCE
45.37-
119GlutarylationIQAVLLPKKTESHKA
EEEEECCCCCHHHCC
72.76-
119CrotonylationIQAVLLPKKTESHKA
EEEEECCCCCHHHCC
72.76-
119OtherIQAVLLPKKTESHKA
EEEEECCCCCHHHCC
72.76-
119N6-crotonyl-L-lysineIQAVLLPKKTESHKA
EEEEECCCCCHHHCC
72.76-
120GlutarylationQAVLLPKKTESHKAK
EEEECCCCCHHHCCC
56.43-
120CrotonylationQAVLLPKKTESHKAK
EEEECCCCCHHHCCC
56.43-
120N6-crotonyl-L-lysineQAVLLPKKTESHKAK
EEEECCCCCHHHCCC
56.43-
121PhosphorylationAVLLPKKTESHKAKS
EEECCCCCHHHCCCC
49.17-
123PhosphorylationLLPKKTESHKAKSK-
ECCCCCHHHCCCCC-
35.20-
125N6-crotonyl-L-lysinePKKTESHKAKSK---
CCCCHHHCCCCC---
67.78-
125CrotonylationPKKTESHKAKSK---
CCCCHHHCCCCC---
67.78-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
2SPhosphorylationKinaseRPS6KA5-Uniprot
121TPhosphorylationKinaseDCAF1-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H2A2C_BOVIN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of H2A2C_BOVIN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2A2C_BOVIN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H2A2C_BOVIN

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Related Literatures of Post-Translational Modification

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